GenomeNet

Database: UniProt
Entry: A0A1F4
LinkDB: A0A1F4
Original site: A0A1F4 
ID   EYS_DROME               Reviewed;        2176 AA.
AC   A0A1F4; Q06PM7; Q400N0; Q6IHY1; Q8MRJ7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JAN-2019, entry version 103.
DE   RecName: Full=Protein eyes shut;
DE   AltName: Full=Protein spacemaker;
GN   Name=eys {ECO:0000312|EMBL:ABJ09588.1,
GN   ECO:0000312|FlyBase:FBgn0031414};
GN   Synonyms=spam {ECO:0000312|EMBL:ABH07112.1}; ORFNames=CG33955;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABJ09588.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLU-521.
RX   PubMed=17011488; DOI=10.1016/j.devcel.2006.08.012;
RA   Husain N., Pellikka M., Hong H., Klimentova T., Choe K.-M.,
RA   Clandinin T.R., Tepass U.;
RT   "The agrin/perlecan-related protein eyes shut is essential for
RT   epithelial lumen formation in the Drosophila retina.";
RL   Dev. Cell 11:483-493(2006).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:ABH07112.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-2176, FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17036004; DOI=10.1038/nature05128;
RA   Zelhof A.C., Hardy R.W., Becker A., Zuker C.S.;
RT   "Transforming the architecture of compound eyes.";
RL   Nature 443:696-699(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4] {ECO:0000305}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAM50220.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1660-2176.
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM50220.1};
RC   TISSUE=Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6] {ECO:0000305, ECO:0000312|EMBL:DAA03484.1}
RP   IDENTIFICATION.
RX   PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA   Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA   Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D.,
RA   Paro R.;
RT   "An integrated gene annotation and transcriptional profiling approach
RT   towards the full gene content of the Drosophila genome.";
RL   Genome Biol. 5:R3.1-R3.17(2003).
RN   [7] {ECO:0000305}
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1471, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Oregon-R; TISSUE=Head {ECO:0000269|PubMed:17893096};
RX   PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA   Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA   Panin V.;
RT   "Identification of N-glycosylated proteins from the central nervous
RT   system of Drosophila melanogaster.";
RL   Glycobiology 17:1388-1403(2007).
CC   -!- FUNCTION: Essential for the formation of matrix-filled
CC       interrhabdomeral space: critical for the formation of epithelial
CC       lumina in the retina. Acts together with prominin (prom) and the
CC       cell adhesion molecule chaoptin (chp) to choreograph the
CC       partitioning of rhabdomeres into an open system.
CC       {ECO:0000269|PubMed:17011488, ECO:0000269|PubMed:17036004}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:17011488,
CC       ECO:0000269|PubMed:17036004}. Note=Secreted by photoreceptor
CC       cells, through the stalk membrane into the interrhabdomeral space
CC       (IRS). Although secreted, lacks a canonical signal sequence and
CC       contains a predicted transmembrane domain. The discrepancy may be
CC       explained by protein cleavage after the transmembrane region.
CC   -!- TISSUE SPECIFICITY: Expressed from the beginning of rhabdomere
CC       biogenesis (48 hours after pupal formation), when it decorates the
CC       entire photoreceptor apical surface.
CC       {ECO:0000269|PubMed:17036004}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryonic, larval, and adult
CC       stages. {ECO:0000269|PubMed:17011488}.
CC   -!- DISRUPTION PHENOTYPE: Flies exhibit a closed rhabdomere system,
CC       rhabdomeres within each ommatidium are fused to each other.
CC       {ECO:0000269|PubMed:17036004}.
CC   -!- SIMILARITY: Belongs to the EYS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DAA03484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ991915; ABJ09588.1; -; mRNA.
DR   EMBL; DQ780942; ABH07112.1; -; mRNA.
DR   EMBL; AE014134; AAZ83988.3; -; Genomic_DNA.
DR   EMBL; AY119566; AAM50220.1; -; mRNA.
DR   EMBL; BK003285; DAA03484.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_001027571.3; NM_001032399.3.
DR   RefSeq; NP_001259924.2; NM_001272995.1.
DR   UniGene; Dm.12205; -.
DR   ProteinModelPortal; A0A1F4; -.
DR   BioGrid; 533487; 3.
DR   STRING; 7227.FBpp0112919; -.
DR   iPTMnet; A0A1F4; -.
DR   PaxDb; A0A1F4; -.
DR   PRIDE; A0A1F4; -.
DR   EnsemblMetazoa; FBtr0344662; FBpp0311004; FBgn0031414.
DR   EnsemblMetazoa; FBtr0344663; FBpp0311005; FBgn0031414.
DR   GeneID; 3771890; -.
DR   KEGG; dme:Dmel_CG33955; -.
DR   CTD; 346007; -.
DR   FlyBase; FBgn0031414; eys.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3509; Eukaryota.
DR   eggNOG; ENOG410XS9U; LUCA.
DR   InParanoid; A0A1F4; -.
DR   KO; K19601; -.
DR   OMA; HCEVDVA; -.
DR   OrthoDB; 115967at2759; -.
DR   PhylomeDB; A0A1F4; -.
DR   GenomeRNAi; 3771890; -.
DR   PRO; PR:A0A1F4; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031414; Expressed in 10 organ(s), highest expression level in head.
DR   ExpressionAtlas; A0A1F4; baseline and differential.
DR   Genevisible; A0A1F4; DM.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097730; C:non-motile cilium; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IMP:FlyBase.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR   GO; GO:0042052; P:rhabdomere development; IMP:UniProtKB.
DR   GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:FlyBase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00179; EGF_CA; 10.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; SSF49899; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; 14.
DR   PROSITE; PS01186; EGF_2; 8.
DR   PROSITE; PS50026; EGF_3; 13.
DR   PROSITE; PS01187; EGF_CA; 4.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Secreted;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   2176       Protein eyes shut.
FT                                /FTId=PRO_0000339236.
FT   TOPO_DOM      1    122       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    123    143       Helical. {ECO:0000255}.
FT   TOPO_DOM    144   2176       Extracellular. {ECO:0000255}.
FT   DOMAIN      144    180       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      182    218       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      220    256       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      258    298       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      300    336       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      338    374       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      376    413       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1018   1054       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1059   1266       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1309   1346       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1353   1549       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1545   1581       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1583   1621       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1692   1879       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1875   1912       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1913   1946       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1952   2166       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   COMPBIAS    484    661       Ser-rich. {ECO:0000255}.
FT   COMPBIAS    812    842       His-rich. {ECO:0000255}.
FT   COMPBIAS    878    980       Pro-rich. {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1165   1165       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1170   1170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1176   1176       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1471   1471       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17893096}.
FT   CARBOHYD   1665   1665       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1861   1861       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1994   1994       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2035   2035       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2099   2099       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    148    158       {ECO:0000255}.
FT   DISULFID    153    168       {ECO:0000255}.
FT   DISULFID    170    179       {ECO:0000255}.
FT   DISULFID    186    197       {ECO:0000255}.
FT   DISULFID    191    206       {ECO:0000255}.
FT   DISULFID    208    217       {ECO:0000255}.
FT   DISULFID    224    235       {ECO:0000255}.
FT   DISULFID    229    244       {ECO:0000255}.
FT   DISULFID    246    255       {ECO:0000255}.
FT   DISULFID    262    276       {ECO:0000255}.
FT   DISULFID    270    286       {ECO:0000255}.
FT   DISULFID    288    297       {ECO:0000255}.
FT   DISULFID    304    315       {ECO:0000255}.
FT   DISULFID    309    324       {ECO:0000255}.
FT   DISULFID    326    335       {ECO:0000255}.
FT   DISULFID    342    353       {ECO:0000255}.
FT   DISULFID    347    362       {ECO:0000255}.
FT   DISULFID    364    373       {ECO:0000255}.
FT   DISULFID    380    392       {ECO:0000255}.
FT   DISULFID    386    401       {ECO:0000255}.
FT   DISULFID    403    412       {ECO:0000255}.
FT   DISULFID   1022   1033       {ECO:0000255}.
FT   DISULFID   1027   1042       {ECO:0000255}.
FT   DISULFID   1044   1053       {ECO:0000255}.
FT   DISULFID   1313   1324       {ECO:0000255}.
FT   DISULFID   1318   1334       {ECO:0000255}.
FT   DISULFID   1336   1345       {ECO:0000255}.
FT   DISULFID   1549   1560       {ECO:0000255}.
FT   DISULFID   1554   1569       {ECO:0000255}.
FT   DISULFID   1571   1580       {ECO:0000255}.
FT   DISULFID   1587   1600       {ECO:0000255}.
FT   DISULFID   1594   1609       {ECO:0000255}.
FT   DISULFID   1611   1620       {ECO:0000255}.
FT   DISULFID   1879   1890       {ECO:0000255}.
FT   DISULFID   1884   1900       {ECO:0000255}.
FT   DISULFID   1902   1911       {ECO:0000255}.
FT   DISULFID   1917   1928       {ECO:0000255}.
FT   DISULFID   1922   1934       {ECO:0000255}.
FT   DISULFID   1936   1945       {ECO:0000255}.
FT   MUTAGEN     521    521       E->K: In eys(734); fails to form an
FT                                interrhabdomeral space.
FT                                {ECO:0000269|PubMed:17011488}.
SQ   SEQUENCE   2176 AA;  234104 MW;  7C21E204FCF3E311 CRC64;
     MSNVHQFDTQ TMAESPQIRR DMGRLCATWP SKDSEDGAGT ALRAATPLTA NGATTTGLSV
     TLAPKDMQRN HLLKMPTATI EKPTITATIA SSSSTSTSTT RKSVTATRSL KLNPNILLPT
     LRILARGLLL PALILAILVG SSQAGFACLS NPCVFGVCID GLNSSYSCYC IDGYTGIQCQ
     TNWDECWSSP CQNGGTCVDG VAYYNCTCPE GFSGSNCEEN VDECMSNPCQ NGGLCRDRTN
     GYICTCQPGY LGSHCELDVA VCETGTGARC QHGGECIEGP GLEFTCDCPA GWHGRICQEE
     INECASSPCQ NGGVCVDKLA AYACACPMGY TGINCEEEIL ICADNPCQNN ALCLMEEGVP
     TCYCVPDYHG EKCEFQYDEC QLGPRCMNGG VCIDGVDTFS CSCPPLLTGM LCECLMVGEE
     SLDCNYTAPA TQSPPRRTTT TSTMAPPTVR PVTPPETTVS PSRASEEVEI IVVTTSAPAE
     VVTSVLSPSS SSSSSEEGVS VEIKTPTVAP PESGSHSISV EQTTAVPAQP EPESEQEPES
     KPHPESESAS ESETETEEEI IPGTTARPPT SRSSSSSEES PSIFTTLPPL PGKPQTSASS
     ESSGEVVTSE EYTTVPHFEV SGSKSESGSE EVTTVRPTAA PSITISVDIT SSGSSSSSSE
     SVEVFTTPAP VFVQRVTTIE TSISIDYVTP TPLPETTTPR VVPVPRPTFA PEPPLDVVET
     TASTHHLWTE VPTTAAPFFT EYPAEVLITT HRTSAGRFTT VQPPAGVTTT SPTEDSSVEL
     PTPHTPQIVV TILDSNEVIP SLITTTGSPT THHHHHHHPH HEAEGTTLQP LEEDEHHHHH
     HHDEFTTPQP VEITTGHPLQ TEDLIGVQEP AVVTTESPFA PAETTVVPVV VPATIAPLGT
     AAPPATPAPV PPATTTPPPS PPSLATETPT LPPTLPPVTL PPVTQPPPTI PPTPPSTQSA
     QTLPPPTSAI NVYTTPDGPP TASQTKPSVT ESSEEVEGTN TVSTGGRGSG GVPEEKAGDV
     DCIKLGCYNG GTCVTTSEGS RCVCRFDRQG PLCELPIIIR NAAFSGDSYV SHRIYKDIGG
     HESLDAVLPM HIQLKVRTRA TNGLIMLAAA QGTKGGHYMA LFLQKGLMQF QFSCGLQTML
     LSELETPVNT GHEITIRAEL DFSRNYTHCN ASLLVNDTLA MSGDQPTWLK LLPPRLHTPE
     AILNTWLHLG GAPQAPIGLI IELPPAQSGS GFTGCLHTLR INGQAREIFG DALDGFGITE
     CGSLACLSSP CRNGAACIKI ETNDLDENGE KAEKWKCKCP TGYMGPTCEI SVCEDNPCQY
     GGTCVQFPGS GYLCLCPLGK HGHYCEHNLE VALPSFSGSV NGLSSFVAYT VPIPLEYSLE
     LSFKILPQTM SQISLLAFFG QSGYHDEKSD HLAVSFIQGY IMLTWNLGAG PRRIFTQKPI
     DFRLDAPRVP YEIKVGRIGR QAWLSVDGKF NITGRSPGSG SRMDVLPILY LGGHEIANFN
     TLPHDLPLHS GFQGCIYDVQ LKAGQVTVPL QETRGVRGRG VGQCGTRECH RHACQHDGAC
     LQHGATFTCI CQEGWYGPLC AQPTNPCDSF NNKCYEDATC VPLVNGYECD CPVGRTGKNC
     EEVIRSLSDV SLTGRRSYLA VRWPYLYDGG DKLGAKRSQM VSYRNFTKKL MPPKPITTPS
     SHFVMKLLNE VEKQRSFSPV PLMGSKSFEE HHRVQFFFIE FQLRPLSERG LLLYFGTLNN
     NQDKKIGFVS LSLQGGVVEF RISGPSNHVT VVRSVRMLAI GEWHKIKMAQ RGRWLTLWVE
     GSASSALAPS AEVLVEPDSL LYIGGLKDVS KLPHNAISGF PIPFRGCVRG LVVSGTRIVL
     NETNIVESRN IRDCDGTACG GDSCESGGHC WLDEKLQPHC ICPEYAKGDR CEYSETCKLI
     PCKNNGRCLR SGRCSCPNGW GGFYCEIAMS KPTTPSFRGN SYLILPPPRI PMKDKRRGPS
     LYVRPREAIQ VSLNFSTIEP DGLLLWSEHE RSKFLGLGLE AGHLKLASNL LGSTNDTVRA
     PASGFIADGA WHWTSVLLDR SRLELQLDGE VIFTERLPEG GRSLGSTTPR STLAGRRKNS
     SKEPTISYED VFYLGGFPNS DSVSRRTKGR FFDPFKGCLQ DIQFGAEPTA IISDFSTYQG
     ENIGSCDLHG DEPLTV
//
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